BBS2_MOUSE
ID BBS2_MOUSE Reviewed; 721 AA.
AC Q9CWF6;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Bardet-Biedl syndrome 2 protein homolog;
GN Name=Bbs2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Swiss Webster / NIH; TISSUE=Fetus;
RX PubMed=11285252; DOI=10.1093/hmg/10.8.865;
RA Nishimura D.Y., Searby C.C., Carmi R., Elbedour K., Van Maldergem L.,
RA Fulton A.B., Lam B.L., Powell B.R., Swiderski R.E., Bugge K.E.,
RA Haider N.B., Kwitek-Black A.E., Ying L., Duhl D.M., Gorman S.M., Heon E.,
RA Iannaccone A., Bonneau D., Biesecker L.G., Jacobson S.G., Stone E.M.,
RA Sheffield V.C.;
RT "Positional cloning of a novel gene on chromosome 16q causing Bardet-Biedl
RT syndrome (BBS2).";
RL Hum. Mol. Genet. 10:865-874(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP IDENTIFICATION IN THE BBSOME COMPLEX.
RX PubMed=22072986; DOI=10.1371/journal.pgen.1002358;
RA Seo S., Zhang Q., Bugge K., Breslow D.K., Searby C.C., Nachury M.V.,
RA Sheffield V.C.;
RT "A novel protein LZTFL1 regulates ciliary trafficking of the BBSome and
RT Smoothened.";
RL PLoS Genet. 7:E1002358-E1002358(2011).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=18317593; DOI=10.1172/jci32357;
RA Rahmouni K., Fath M.A., Seo S., Thedens D.R., Berry C.J., Weiss R.,
RA Nishimura D.Y., Sheffield V.C.;
RT "Leptin resistance contributes to obesity and hypertension in mouse models
RT of Bardet-Biedl syndrome.";
RL J. Clin. Invest. 118:1458-1467(2008).
CC -!- FUNCTION: The BBSome complex is thought to function as a coat complex
CC required for sorting of specific membrane proteins to the primary
CC cilia. The BBSome complex is required for ciliogenesis but is
CC dispensable for centriolar satellite function. This ciliogenic function
CC is mediated in part by the Rab8 GDP/GTP exchange factor, which
CC localizes to the basal body and contacts the BBSome. Rab8(GTP) enters
CC the primary cilium and promotes extension of the ciliary membrane.
CC Firstly the BBSome associates with the ciliary membrane and binds to
CC RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the
CC Rab8-GTP localizes to the cilium and promotes docking and fusion of
CC carrier vesicles to the base of the ciliary membrane. The BBSome
CC complex, together with the LTZL1, controls SMO ciliary trafficking and
CC contributes to the sonic hedgehog (SHH) pathway regulation. Required
CC for proper BBSome complex assembly and its ciliary localization (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5,
CC BBS7, BBS8/TTC8, BBS9 and BBIP10. Interacts (via C-terminus) with BBS7.
CC Interacts (via coiled coil domain) with MKKS. Interacts with CCDC28B
CC (By similarity). Interacts with DLEC1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9BXC9, ECO:0000269|PubMed:22072986}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000250}.
CC Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriolar satellite {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: In mice obesity is associated with
CC hyperleptinemia and resistance to the anorectic and weight-reducing
CC effects of leptinan mice are resistant to the metabolic actions of
CC leptin. {ECO:0000269|PubMed:18317593}.
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DR EMBL; AF342737; AAK28553.1; -; mRNA.
DR EMBL; AK010779; BAB27176.1; -; mRNA.
DR EMBL; BC057184; AAH57184.1; -; mRNA.
DR CCDS; CCDS40434.1; -.
DR RefSeq; NP_080392.1; NM_026116.2.
DR AlphaFoldDB; Q9CWF6; -.
DR SMR; Q9CWF6; -.
DR BioGRID; 212145; 4.
DR ComplexPortal; CPX-1909; BBSome complex.
DR DIP; DIP-60351N; -.
DR IntAct; Q9CWF6; 12.
DR STRING; 10090.ENSMUSP00000034206; -.
DR iPTMnet; Q9CWF6; -.
DR PhosphoSitePlus; Q9CWF6; -.
DR MaxQB; Q9CWF6; -.
DR PaxDb; Q9CWF6; -.
DR PRIDE; Q9CWF6; -.
DR ProteomicsDB; 273732; -.
DR Antibodypedia; 28577; 116 antibodies from 23 providers.
DR DNASU; 67378; -.
DR Ensembl; ENSMUST00000034206; ENSMUSP00000034206; ENSMUSG00000031755.
DR GeneID; 67378; -.
DR KEGG; mmu:67378; -.
DR UCSC; uc009mvs.1; mouse.
DR CTD; 583; -.
DR MGI; MGI:2135267; Bbs2.
DR VEuPathDB; HostDB:ENSMUSG00000031755; -.
DR eggNOG; ENOG502QPWU; Eukaryota.
DR GeneTree; ENSGT00390000017113; -.
DR HOGENOM; CLU_023359_0_0_1; -.
DR InParanoid; Q9CWF6; -.
DR OMA; IKVDEYH; -.
DR OrthoDB; 327831at2759; -.
DR PhylomeDB; Q9CWF6; -.
DR TreeFam; TF313236; -.
DR Reactome; R-MMU-5620922; BBSome-mediated cargo-targeting to cilium.
DR BioGRID-ORCS; 67378; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Bbs2; mouse.
DR PRO; PR:Q9CWF6; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9CWF6; protein.
DR Bgee; ENSMUSG00000031755; Expressed in retinal neural layer and 222 other tissues.
DR Genevisible; Q9CWF6; MM.
DR GO; GO:0034464; C:BBSome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; ISO:MGI.
DR GO; GO:0060170; C:ciliary membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005902; C:microvillus; IDA:MGI.
DR GO; GO:0031514; C:motile cilium; IMP:BHF-UCL.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0032420; C:stereocilium; IDA:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0030534; P:adult behavior; IMP:MGI.
DR GO; GO:0014824; P:artery smooth muscle contraction; IMP:MGI.
DR GO; GO:0048854; P:brain morphogenesis; IMP:MGI.
DR GO; GO:0051216; P:cartilage development; IMP:MGI.
DR GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR GO; GO:0060271; P:cilium assembly; IMP:BHF-UCL.
DR GO; GO:0045444; P:fat cell differentiation; IEP:BHF-UCL.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; ISO:MGI.
DR GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR GO; GO:0033210; P:leptin-mediated signaling pathway; IMP:MGI.
DR GO; GO:0038108; P:negative regulation of appetite by leptin-mediated signaling pathway; IMP:BHF-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR GO; GO:0040015; P:negative regulation of multicellular organism growth; IMP:MGI.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:MGI.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:MGI.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:1903441; P:protein localization to ciliary membrane; ISO:MGI.
DR GO; GO:0033365; P:protein localization to organelle; IDA:BHF-UCL.
DR GO; GO:0060296; P:regulation of cilium beat frequency involved in ciliary motility; IMP:BHF-UCL.
DR GO; GO:0044321; P:response to leptin; IMP:MGI.
DR GO; GO:0007288; P:sperm axoneme assembly; IMP:MGI.
DR GO; GO:0021756; P:striatum development; IMP:MGI.
DR GO; GO:0042311; P:vasodilation; IMP:MGI.
DR GO; GO:0007601; P:visual perception; ISS:UniProtKB.
DR InterPro; IPR016616; Bardet-Biedl_syndrome_2_prot.
DR InterPro; IPR029333; BBS2_C.
DR InterPro; IPR029429; BBS2_Mid.
DR InterPro; IPR029430; BBS2_N.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR32465; PTHR32465; 1.
DR Pfam; PF14782; BBS2_C; 1.
DR Pfam; PF14783; BBS2_Mid; 1.
DR Pfam; PF14781; BBS2_N; 1.
DR PIRSF; PIRSF013684; BBS2; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cilium; Cilium biogenesis/degradation;
KW Coiled coil; Cytoplasm; Cytoskeleton; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..721
FT /note="Bardet-Biedl syndrome 2 protein homolog"
FT /id="PRO_0000064844"
FT COILED 325..369
FT /evidence="ECO:0000255"
SQ SEQUENCE 721 AA; 79932 MW; C91D9B7834B614F4 CRC64;
MLLPVFTLKL RHKISPRMVA IGRYDGTHPC LAAATQAGKV FIHNPHTRSQ HFSASRVFQS
PLESDVSLLN INQTVSCLGS GVLNPELGYD TLLVGTQTSL LAYDIYNNSD LFYREVSDGA
NAIVLGTLGD IAPPLAIIGG NCALQGFDHE GNDLFWTVTG DNVHSLALCD FDGDGKTELL
VGSEDFDIRV FKEDEIVAEM TETEIVTSLC PMYGSRFGYA LSNGTVGVYD KTARYWRIKS
KNHAMSIHAF DINSDGVCEL ITGWSNGKVD ARSDRTGEVI FKDNFSSAVA GVVEGDYRMD
GHVQLICCSV DGEIRGYLPG TAEMKGNLLD TSVEQDLIRE LSQKKQNLLL ELRNYEESTK
AELSSPLNEA DGQKGIIPAN TRLHTALSVN MGNDLQDAHA ELGISTSNDT IIRAVLIFAE
GIFVGESHVV HPSIHNLSSS LRVPITPPKD VPVDLHLKTF VGYRSSTQFH VFELTRQLPR
FTMYALTSPD AASEPVSYVN FSVAERTQRM VTWLNQNFLL PEDSNVQNSP FHVCFTSLRN
GGQLYIKMKQ SGEITVNTDD IDLAGDIIQS IASFFAIEDL QVEADFPVYF EELRKVLVKV
DEYHSVHQKL SADMADNSNL IRSLLVRAED ARLMRDMKTM KSRYMELYDL NKDLLNGYKI
RCNNHTELLG NLKAVNQAIQ RAGRLRVGKP KNQVISACRD AIRSNNINTL FRIMRVGTAP
S
